dbPTM

DNLI1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	DNLI1_HUMAN
UniProt AC	P18858
Protein Name	DNA ligase 1
Gene Name	LIG1
Organism	Homo sapiens (Human).
Sequence Length	919
Subcellular Localization	Nucleus.
Protein Description	DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair..
Protein Sequence	MQRSIMSFFHPKKEGKAKKPEKEASNSSRETEPPPKAALKEWNGVVSESDSPVKRPGRKAARVLGSEGEEEDEALSPAKGQKPALDCSQVSPPRPATSPENNASLSDTSPMDSSPSGIPKRRTARKQLPKRTIQEVLEEQSEDEDREAKRKKEEEEEETPKESLTEAEVATEKEGEDGDQPTTPPKPLKTSKAETPTESVSEPEVATKQELQEEEEQTKPPRRAPKTLSSFFTPRKPAVKKEVKEEEPGAPGKEGAAEGPLDPSGYNPAKNNYHPVEDACWKPGQKVPYLAVARTFEKIEEVSARLRMVETLSNLLRSVVALSPPDLLPVLYLSLNHLGPPQQGLELGVGDGVLLKAVAQATGRQLESVRAEAAEKGDVGLVAENSRSTQRLMLPPPPLTASGVFSKFRDIARLTGSASTAKKIDIIKGLFVACRHSEARFIARSLSGRLRLGLAEQSVLAALSQAVSLTPPGQEFPPAMVDAGKGKTAEARKTWLEEQGMILKQTFCEVPDLDRIIPVLLEHGLERLPEHCKLSPGIPLKPMLAHPTRGISEVLKRFEEAAFTCEYKYDGQRAQIHALEGGEVKIFSRNQEDNTGKYPDIISRIPKIKLPSVTSFILDTEAVAWDREKKQIQPFQVLTTRKRKEVDASEIQVQVCLYAFDLIYLNGESLVREPLSRRRQLLRENFVETEGEFVFATSLDTKDIEQIAEFLEQSVKDSCEGLMVKTLDVDATYEIAKRSHNWLKLKKDYLDGVGDTLDLVVIGAYLGRGKRAGRYGGFLLASYDEDSEELQAICKLGTGFSDEELEEHHQSLKALVLPSPRPYVRIDGAVIPDHWLDPSAVWEVKCADLSLSPIYPAARGLVDSDKGISLRFPRFIRVREDKQPEQATTSAQVACLYRKQSQIQNQQGEDSGSDPEDTY

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
4	Phosphorylation	----MQRSIMSFFHP ----CCCCHHHHCCC	13.02	30576142
7	Phosphorylation	-MQRSIMSFFHPKKE -CCCCHHHHCCCCCC	24.08	28555341
17 (in isoform 3)	Phosphorylation	-	35.64	25849741
19 (in isoform 3)	Phosphorylation	-	64.37	25849741
21 (in isoform 3)	Phosphorylation	-	72.85	25849741
27	Phosphorylation	PEKEASNSSRETEPP CCHHCCCCCCCCCCC	28.42	25627689
28	Phosphorylation	EKEASNSSRETEPPP CHHCCCCCCCCCCCC	38.08	28985074
40	Ubiquitination	PPPKAALKEWNGVVS CCCHHHHHHHCCCCC	56.83	-
47	Phosphorylation	KEWNGVVSESDSPVK HHHCCCCCCCCCCCC	29.04	23927012
49	Phosphorylation	WNGVVSESDSPVKRP HCCCCCCCCCCCCCC	35.56	22167270
51	Phosphorylation	GVVSESDSPVKRPGR CCCCCCCCCCCCCCH	40.65	19664994
66	Phosphorylation	KAARVLGSEGEEEDE HHHHHHCCCCCHHCC	37.96	19664994
76	Phosphorylation	EEEDEALSPAKGQKP CHHCCCCCCCCCCCC	29.84	19664994
79	Ubiquitination	DEALSPAKGQKPALD CCCCCCCCCCCCCCC	66.32	-
88	Phosphorylation	QKPALDCSQVSPPRP CCCCCCCCCCCCCCC	33.03	23401153
91	Phosphorylation	ALDCSQVSPPRPATS CCCCCCCCCCCCCCC	22.88	19223468
97	Phosphorylation	VSPPRPATSPENNAS CCCCCCCCCCCCCCC	47.71	30278072
98	Phosphorylation	SPPRPATSPENNASL CCCCCCCCCCCCCCC	32.11	30278072
104	Phosphorylation	TSPENNASLSDTSPM CCCCCCCCCCCCCCC	30.45	30278072
106	Phosphorylation	PENNASLSDTSPMDS CCCCCCCCCCCCCCC	36.03	30278072
108	Phosphorylation	NNASLSDTSPMDSSP CCCCCCCCCCCCCCC	31.21	30278072
109	Phosphorylation	NASLSDTSPMDSSPS CCCCCCCCCCCCCCC	24.18	25159151
113	Phosphorylation	SDTSPMDSSPSGIPK CCCCCCCCCCCCCCC	37.59	23927012
114	Phosphorylation	DTSPMDSSPSGIPKR CCCCCCCCCCCCCCH	20.86	25159151
116	Phosphorylation	SPMDSSPSGIPKRRT CCCCCCCCCCCCHHH	51.83	23927012
132	Phosphorylation	RKQLPKRTIQEVLEE HHHCCHHHHHHHHHH	32.89	23927012
132 (in isoform 3)	Phosphorylation	-	32.89	25849741
141	Phosphorylation	QEVLEEQSEDEDREA HHHHHHCCCHHHHHH	50.74	19664994
146	Methylation	EQSEDEDREAKRKKE HCCCHHHHHHHHHHH	43.66	115482091
159	Phosphorylation	KEEEEEETPKESLTE HHHHHHCCCHHHCCH	42.83	23186163
163	Phosphorylation	EEETPKESLTEAEVA HHCCCHHHCCHHHHC	46.87	25159151
165	Phosphorylation	ETPKESLTEAEVATE CCCHHHCCHHHHCCC	42.29	21815630
171	Phosphorylation	LTEAEVATEKEGEDG CCHHHHCCCCCCCCC	53.41	22167270
182	Phosphorylation	GEDGDQPTTPPKPLK CCCCCCCCCCCCCCC	46.42	29255136
183	Phosphorylation	EDGDQPTTPPKPLKT CCCCCCCCCCCCCCC	44.25	29255136
188	Ubiquitination	PTTPPKPLKTSKAET CCCCCCCCCCCCCCC	13.59	-
190	Phosphorylation	TPPKPLKTSKAETPT CCCCCCCCCCCCCCC	43.04	28176443
191	Phosphorylation	PPKPLKTSKAETPTE CCCCCCCCCCCCCCC	28.42	28176443
192	Ubiquitination	PKPLKTSKAETPTES CCCCCCCCCCCCCCC	56.31	-
195	Ubiquitination	LKTSKAETPTESVSE CCCCCCCCCCCCCCC	40.13	-
195	Phosphorylation	LKTSKAETPTESVSE CCCCCCCCCCCCCCC	40.13	19664994
197	Phosphorylation	TSKAETPTESVSEPE CCCCCCCCCCCCCHH	48.59	22167270
199	Phosphorylation	KAETPTESVSEPEVA CCCCCCCCCCCHHHH	33.16	29255136
201	Phosphorylation	ETPTESVSEPEVATK CCCCCCCCCHHHHCH	57.63	19664994
207	Phosphorylation	VSEPEVATKQELQEE CCCHHHHCHHHHHHH	38.14	29255136
218	Phosphorylation	LQEEEEQTKPPRRAP HHHHHHHCCCCCCCC	49.12	26074081
219	Acetylation	QEEEEQTKPPRRAPK HHHHHHCCCCCCCCC	53.36	25953088
219	Ubiquitination	QEEEEQTKPPRRAPK HHHHHHCCCCCCCCC	53.36	-
226	Ubiquitination	KPPRRAPKTLSSFFT CCCCCCCCCHHHCCC	62.20	21890473
226	Acetylation	KPPRRAPKTLSSFFT CCCCCCCCCHHHCCC	62.20	-
226	Ubiquitination	KPPRRAPKTLSSFFT CCCCCCCCCHHHCCC	62.20	21890473
226	Ubiquitination	KPPRRAPKTLSSFFT CCCCCCCCCHHHCCC	62.20	21890473
227	Phosphorylation	PPRRAPKTLSSFFTP CCCCCCCCHHHCCCC	30.71	20068231
229	Phosphorylation	RRAPKTLSSFFTPRK CCCCCCHHHCCCCCC	30.26	23927012
230	Phosphorylation	RAPKTLSSFFTPRKP CCCCCHHHCCCCCCC	27.73	30266825
233	Phosphorylation	KTLSSFFTPRKPAVK CCHHHCCCCCCCCCC	21.85	30266825
240	Sumoylation	TPRKPAVKKEVKEEE CCCCCCCCHHHHCCC	45.37	-
244	Sumoylation	PAVKKEVKEEEPGAP CCCCHHHHCCCCCCC	61.57	-
244	Sumoylation	PAVKKEVKEEEPGAP CCCCHHHHCCCCCCC	61.57	-
244	Ubiquitination	PAVKKEVKEEEPGAP CCCCHHHHCCCCCCC	61.57	-
255	Ubiquitination	PGAPGKEGAAEGPLD CCCCCCCCCCCCCCC	33.31	-
267	Ubiquitination	PLDPSGYNPAKNNYH CCCCCCCCCCCCCCC	33.31	-
270	Ubiquitination	PSGYNPAKNNYHPVE CCCCCCCCCCCCCCC	47.16	-
282	Ubiquitination	PVEDACWKPGQKVPY CCCCCCCCCCCCCCE	38.87	-
286	Ubiquitination	ACWKPGQKVPYLAVA CCCCCCCCCCEEEEE	51.60	-
298	Ubiquitination	AVARTFEKIEEVSAR EEEECHHHHHHHHHH	51.75	-
303	Phosphorylation	FEKIEEVSARLRMVE HHHHHHHHHHHHHHH	15.79	26074081
311	Phosphorylation	ARLRMVETLSNLLRS HHHHHHHHHHHHHHH	24.87	20068231
313	Phosphorylation	LRMVETLSNLLRSVV HHHHHHHHHHHHHHH	32.62	20068231
318	Phosphorylation	TLSNLLRSVVALSPP HHHHHHHHHHHCCCC	22.40	26074081
323	Phosphorylation	LRSVVALSPPDLLPV HHHHHHCCCCHHHHH	25.34	26074081
345	Ubiquitination	LGPPQQGLELGVGDG CCCCCCCCCCCCCCH	4.22	-
376	Ubiquitination	VRAEAAEKGDVGLVA HHHHHHHHCCCEEEE	56.54	-
376	Ubiquitination	VRAEAAEKGDVGLVA HHHHHHHHCCCEEEE	56.54	21906983
393	Sulfoxidation	SRSTQRLMLPPPPLT CCCCCCCCCCCCCCC	6.02	21406390
397	Ubiquitination	QRLMLPPPPLTASGV CCCCCCCCCCCCCHH	34.29	-
406	Phosphorylation	LTASGVFSKFRDIAR CCCCHHHHHHHHHHH	28.60	20068231
407	Ubiquitination	TASGVFSKFRDIARL CCCHHHHHHHHHHHH	32.71	21890473
407	Ubiquitination	TASGVFSKFRDIARL CCCHHHHHHHHHHHH	32.71	21890473
407	Ubiquitination	TASGVFSKFRDIARL CCCHHHHHHHHHHHH	32.71	21890473
417	Phosphorylation	DIARLTGSASTAKKI HHHHHHCCCHHHHHH	17.51	24719451
419	Phosphorylation	ARLTGSASTAKKIDI HHHHCCCHHHHHHHH	30.51	28851738
420	Phosphorylation	RLTGSASTAKKIDII HHHCCCHHHHHHHHH	42.06	28851738
422	Ubiquitination	TGSASTAKKIDIIKG HCCCHHHHHHHHHHH	50.80	21906983
428	Ubiquitination	AKKIDIIKGLFVACR HHHHHHHHHHHHHHC	50.31	-
437	Phosphorylation	LFVACRHSEARFIAR HHHHHCCCHHHHHHH	17.38	21712546
445	Phosphorylation	EARFIARSLSGRLRL HHHHHHHHHCCCHHH	20.19	21712546
447	Phosphorylation	RFIARSLSGRLRLGL HHHHHHHCCCHHHCH	24.10	21712546
493	Ubiquitination	GKTAEARKTWLEEQG CCCHHHHHHHHHHHC	51.61	-
506	Phosphorylation	QGMILKQTFCEVPDL HCCEEEEEECCCCCH	28.76	20860994
510	Ubiquitination	LKQTFCEVPDLDRII EEEEECCCCCHHHHH	4.74	-
525	Ubiquitination	PVLLEHGLERLPEHC HHHHHCHHHHCHHHC	3.60	-
533	Ubiquitination	ERLPEHCKLSPGIPL HHCHHHCCCCCCCCC	54.64	-
535	Phosphorylation	LPEHCKLSPGIPLKP CHHHCCCCCCCCCCC	13.43	20068231
541	Ubiquitination	LSPGIPLKPMLAHPT CCCCCCCCCCCCCCC	24.03	-
548	Phosphorylation	KPMLAHPTRGISEVL CCCCCCCCCCHHHHH	31.49	20068231
552	Phosphorylation	AHPTRGISEVLKRFE CCCCCCHHHHHHHHH	25.20	23312004
556	Ubiquitination	RGISEVLKRFEEAAF CCHHHHHHHHHHHHC	61.28	-
568	Ubiquitination	AAFTCEYKYDGQRAQ HHCEEEEEECCCEEE	17.99	-
585	Ubiquitination	ALEGGEVKIFSRNQE EECCCEEEEEECCCC	33.46	-
597	Acetylation	NQEDNTGKYPDIISR CCCCCCCCCCHHHHC	52.12	25953088
597	Ubiquitination	NQEDNTGKYPDIISR CCCCCCCCCCHHHHC	52.12	-
599	Ubiquitination	EDNTGKYPDIISRIP CCCCCCCCHHHHCCC	29.79	-
630	Sumoylation	VAWDREKKQIQPFQV HCCHHHHCCCCCEEE	48.13	-
630	Sumoylation	VAWDREKKQIQPFQV HCCHHHHCCCCCEEE	48.13	-
630	Ubiquitination	VAWDREKKQIQPFQV HCCHHHHCCCCCEEE	48.13	-
639	Phosphorylation	IQPFQVLTTRKRKEV CCCEEEEECCCCCCC	26.21	-
697	Phosphorylation	EGEFVFATSLDTKDI CCEEEEEEECCHHCH	20.54	28787133
698	Phosphorylation	GEFVFATSLDTKDIE CEEEEEEECCHHCHH	22.33	28787133
701	Phosphorylation	VFATSLDTKDIEQIA EEEEECCHHCHHHHH	35.59	28787133
706	Ubiquitination	LDTKDIEQIAEFLEQ CCHHCHHHHHHHHHH	40.29	-
713	Ubiquitination	QIAEFLEQSVKDSCE HHHHHHHHHHHHHCC	56.52	-
714	Phosphorylation	IAEFLEQSVKDSCEG HHHHHHHHHHHHCCC	23.04	20068231
737	Ubiquitination	DATYEIAKRSHNWLK CCCHHHHHHCCCHHH	61.16	-
744	Ubiquitination	KRSHNWLKLKKDYLD HHCCCHHHHCHHHHC	50.29	-
764	Methylation	LDLVVIGAYLGRGKR EEEEEEEEHHCCCCC	5.81	-
764	Ubiquitination	LDLVVIGAYLGRGKR EEEEEEEEHHCCCCC	5.81	-
795	Methylation	EELQAICKLGTGFSD HHHHHHHHHCCCCCH	43.78	23583077
795	Ubiquitination	EELQAICKLGTGFSD HHHHHHHHHCCCCCH	43.78	-
798	Phosphorylation	QAICKLGTGFSDEEL HHHHHHCCCCCHHHH	45.55	28450419
801	Phosphorylation	CKLGTGFSDEELEEH HHHCCCCCHHHHHHH	45.52	23401153
811	Phosphorylation	ELEEHHQSLKALVLP HHHHHHHHHHHHHCC	27.72	26074081
813	Ubiquitination	EEHHQSLKALVLPSP HHHHHHHHHHHCCCC	44.94	-
819	Phosphorylation	LKALVLPSPRPYVRI HHHHHCCCCCCEEEE	29.40	30266825
823	Phosphorylation	VLPSPRPYVRIDGAV HCCCCCCEEEECCEE	12.02	22199227
835	Ubiquitination	GAVIPDHWLDPSAVW CEECCCCCCCHHHEE	15.16	-
866	Acetylation	RGLVDSDKGISLRFP CCCCCCCCCCCCCCC	63.19	25953088
866	Ubiquitination	RGLVDSDKGISLRFP CCCCCCCCCCCCCCC	63.19	-
888	Phosphorylation	DKQPEQATTSAQVAC CCCCCCCCHHHHHHH	22.45	26074081
889	Phosphorylation	KQPEQATTSAQVACL CCCCCCCHHHHHHHH	25.69	26074081
890	Phosphorylation	QPEQATTSAQVACLY CCCCCCHHHHHHHHH	16.61	26074081
897	Phosphorylation	SAQVACLYRKQSQIQ HHHHHHHHHHHHHHH	18.69	26074081
901	Phosphorylation	ACLYRKQSQIQNQQG HHHHHHHHHHHHCCC	32.08	22167270
911	Phosphorylation	QNQQGEDSGSDPEDT HHCCCCCCCCCCCCC	35.57	22167270
913	Phosphorylation	QQGEDSGSDPEDTY- CCCCCCCCCCCCCC-	54.68	22167270
918	Phosphorylation	SGSDPEDTY------ CCCCCCCCC------	29.48	22167270
919	Phosphorylation	GSDPEDTY------- CCCCCCCC-------	28.95	22167270

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
51	S	Phosphorylation	Kinase	CDK2	P24941	PSP
66	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
66	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
66	S	Phosphorylation	Kinase	CK2_GROUP	-	PhosphoELM
76	S	Phosphorylation	Kinase	CDK1	P06493	PSP
76	S	Phosphorylation	Kinase	CDK2	P24941	PSP
76	S	Phosphorylation	Kinase	CHEK1	O14757	GPS
91	S	Phosphorylation	Kinase	CDK2	P24941	PSP
233	T	Phosphorylation	Kinase	CDK2	P24941	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of DNLI1_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of DNLI1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MRE11_HUMAN	MRE11A	physical	8530104
CTF18_HUMAN	CHTF18	physical	26344197
FEN1_HUMAN	FEN1	physical	26344197
STKL1_HUMAN	STKLD1	physical	26344197
UHRF1_HUMAN	UHRF1	physical	28803780

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00290	Bleomycin

Regulatory Network of DNLI1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49; SER-51; SER-66;SER-76; SER-141; THR-195; SER-201; SER-229; THR-233; SER-911 ANDSER-913, AND MASS SPECTROMETRY.	19690332 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51; SER-66; SER-76;SER-141; THR-195; SER-201; THR-233; SER-911 AND SER-913, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; Anal. Sci. 24:161-166(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49; SER-51 AND SER-141,AND MASS SPECTROMETRY.	18187866 [Abstract]
"Quantitative phosphoproteome profiling of Wnt3a-mediated signalingnetwork: indicating the involvement of ribonucleoside-diphosphatereductase M2 subunit phosphorylation at residue serine 20 in canonicalWnt signal transduction."; Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S.,Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.; Mol. Cell. Proteomics 6:1952-1967(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66 AND SER-76, AND MASSSPECTROMETRY.	17693683 [Abstract]
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230, AND MASSSPECTROMETRY.	17924679 [Abstract]
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51; SER-66; SER-76;THR-195 AND THR-233, AND MASS SPECTROMETRY.	16964243 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49; SER-66; SER-76;SER-141; THR-195; SER-201 AND THR-233, AND MASS SPECTROMETRY.	17081983 [Abstract]
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66; SER-76; SER-141;THR-195 AND SER-911, AND MASS SPECTROMETRY.	15302935 [Abstract]
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-233, AND MASSSPECTROMETRY.	18220336 [Abstract]
Ubiquitylation
Reference	PubMed
"Proteomic analysis of ubiquitinated proteins in normal hepatocytecell line Chang liver cells."; Tan F., Lu L., Cai Y., Wang J., Xie Y., Wang L., Gong Y., Xu B.-E.,Wu J., Luo Y., Qiang B., Yuan J., Sun X., Peng X.; Proteomics 8:2885-2896(2008). Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-422, AND MASSSPECTROMETRY.	18655026 [Abstract]